A UV resonance Raman spectrometer will be constructed which is continuously tunable inthe Uv and visible spectral region between 2200-8000 angstroms. A series of studies will be initiated to demonstrate the utility of UV resonance Raman spectroscopy as a selective and sensitive probe of protein conformation. The objective of this work is to develop a spectroscopic technique which can selectively and sequentially examine the vibrational spectra of individually aromatic amino acids in proteins. The technique will monitor conformation and environment by examining individual aromatic amino acid resonance Raman fundamental and overtone vibrational frequencies, and resonance Raman excitation profiles. A number of model studies will calibrate the sensitivity of Raman intensitites to aromatic amino acid environment. The first protein study will utilize both UV and visible resonance Raman spectroscopy in a concerted investigation of the hemoglobin cooperativity mechanism. Changes in globin conformation as expressed in alterations in aromatic amino acid environment will be correlated with heme geometric changes and alterations of iron-ligand bonding and ligand-globin interactions. UV resonance Raman spectroscopy will subsequently be extended to non-heme proteins. Development of Uv resonance Raman spectroscopy will be useful for all biological molecules with Uv absorption bands such as proteins, DNA, flavins, etc. The selectivity of the technique makes it applicable for aqueous solution studies as well as to "in vivo" studies. This technique will be useful in biomedical research as a probe of biomolecular structure and function.